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5D2M

Complex between human SUMO2-RANGAP1, UBC9 and ZNF451

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000795cellular_componentsynaptonemal complex
A0001221molecular_functiontranscription coregulator binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005643cellular_componentnuclear pore
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0007059biological_processchromosome segregation
A0007084biological_processmitotic nuclear membrane reassembly
A0008134molecular_functiontranscription factor binding
A0016605cellular_componentPML body
A0016740molecular_functiontransferase activity
A0016925biological_processprotein sumoylation
A0019787molecular_functionubiquitin-like protein transferase activity
A0019789molecular_functionSUMO transferase activity
A0019899molecular_functionenzyme binding
A0030335biological_processpositive regulation of cell migration
A0032446biological_processprotein modification by small protein conjugation
A0036211biological_processprotein modification process
A0044388molecular_functionsmall protein activating enzyme binding
A0045892biological_processnegative regulation of DNA-templated transcription
A0048471cellular_componentperinuclear region of cytoplasm
A0051168biological_processnuclear export
A0051301biological_processcell division
A0061656molecular_functionSUMO conjugating enzyme activity
A0071535molecular_functionRING-like zinc finger domain binding
A0106068cellular_componentSUMO ligase complex
A1903755biological_processpositive regulation of SUMO transferase activity
A1990234cellular_componenttransferase complex
C0005096molecular_functionGTPase activator activity
C0007165biological_processsignal transduction
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0000795cellular_componentsynaptonemal complex
D0001221molecular_functiontranscription coregulator binding
D0003723molecular_functionRNA binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005635cellular_componentnuclear envelope
D0005643cellular_componentnuclear pore
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006511biological_processubiquitin-dependent protein catabolic process
D0007059biological_processchromosome segregation
D0007084biological_processmitotic nuclear membrane reassembly
D0008134molecular_functiontranscription factor binding
D0016605cellular_componentPML body
D0016740molecular_functiontransferase activity
D0016925biological_processprotein sumoylation
D0019787molecular_functionubiquitin-like protein transferase activity
D0019789molecular_functionSUMO transferase activity
D0019899molecular_functionenzyme binding
D0030335biological_processpositive regulation of cell migration
D0032446biological_processprotein modification by small protein conjugation
D0036211biological_processprotein modification process
D0044388molecular_functionsmall protein activating enzyme binding
D0045892biological_processnegative regulation of DNA-templated transcription
D0048471cellular_componentperinuclear region of cytoplasm
D0051168biological_processnuclear export
D0051301biological_processcell division
D0061656molecular_functionSUMO conjugating enzyme activity
D0071535molecular_functionRING-like zinc finger domain binding
D0106068cellular_componentSUMO ligase complex
D1903755biological_processpositive regulation of SUMO transferase activity
D1990234cellular_componenttransferase complex
F0005096molecular_functionGTPase activator activity
F0007165biological_processsignal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue EDO A 301
ChainResidue
ALYS18
AASP19
AHOH432
AHOH434
AHOH471
ETHR83
GARG40

site_idAC2
Number of Residues1
Detailsbinding site for residue EDO C 601
ChainResidue
CGLY521

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO C 602
ChainResidue
CASP482
CHOH764
DHIS20
DHOH265
CLYS481

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO F 601
ChainResidue
FGLY521
FLEU522
FLYS524
FHOH713

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO F 602
ChainResidue
FTYR536
FCYS573
FSER574
FPHE575
FALA576

site_idAC6
Number of Residues12
Detailsbinding site for Di-peptide GLY E 93 and LYS F 524
ChainResidue
DASN85
DCYS93
DASP127
DPRO128
DALA129
DHOH239
EGLY92
FLEU523
FSER525
FEDO601
FHOH707
FHOH785

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. FHPNVyps.GtVCLsiL
ChainResidueDetails
APHE82-LEU97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Hydrophobic interaction with UBE2I => ECO:0000250
ChainResidueDetails
CPHE562
CLYS565
FPHE562
FLYS565

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15037602, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
ChainResidueDetails
CSER428
FSER428
ALEU57
EGLY93
DVAL25
DLEU57

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
CSER435
FSER435

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
CTHR436
FTHR436

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15037602, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER442
FSER442

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
CLYS524
FLYS524

site_idSWS_FT_FI7
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS452
DLYS18
CLYS586
FLYS452
FLYS586

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS524
FLYS524
DLYS101

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS48
DLYS48

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS49
DLYS49

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PDB entries from 2024-07-24

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